Probing amyloid formation of intrinsically disordered proteins (IDPs) in aqueous solutions with ionic liquids (ILs) could help identify the IL–IDP interactions causing the process in this media. Takekiyo et al. report that ethylammonium nitrate (EAN) initiates the formation of intermolecular β‐sheet structure – amyloid‐like aggregates – of α‐synuclein. The cations and anions of EAN function as charges to mask side chains, leading to the formation of a polyproline II helix that assists the formation of α‐synuclein aggregates. The present results could help develop promoting agents for amyloid aggregates in biomaterials science. (DOI: 10.1002/bip.23352)

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用离子液体（IL）探测水溶液中固有无序蛋白（IDP）的淀粉样蛋白形成可能有助于鉴定引起该过程的IL-IDP相互作用。Takekiyo等。报告指出，硝酸乙基铵（EAN）引发了α-突触核蛋白的分子间β-折叠结构（淀粉样样聚集体）的形成。EAN的阳离子和阴离子起掩盖侧链电荷的作用，从而导致形成聚脯氨酸II螺旋，从而有助于α-突触核蛋白聚集体的形成。目前的结果可能有助于开发生物材料科学中淀粉样聚集体的促进剂。（DOI：10.1002 / bip.23352）